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Database: UniProt
Entry: F6PM43_MONDO
LinkDB: F6PM43_MONDO
Original site: F6PM43_MONDO 
ID   F6PM43_MONDO            Unreviewed;      1198 AA.
AC   F6PM43;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Tight junction protein 2 {ECO:0000313|Ensembl:ENSMODP00000003579.4};
GN   Name=TJP2 {ECO:0000313|Ensembl:ENSMODP00000003579.4};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000003579.4, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000003579.4, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000003579.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
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DR   AlphaFoldDB; F6PM43; -.
DR   STRING; 13616.ENSMODP00000003579; -.
DR   Ensembl; ENSMODT00000003657.4; ENSMODP00000003579.4; ENSMODG00000002938.4.
DR   eggNOG; KOG3580; Eukaryota.
DR   GeneTree; ENSGT00940000155164; -.
DR   HOGENOM; CLU_006234_1_0_1; -.
DR   InParanoid; F6PM43; -.
DR   OMA; RQRHSKI; -.
DR   TreeFam; TF315957; -.
DR   Proteomes; UP000002280; Chromosome 6.
DR   Bgee; ENSMODG00000002938; Expressed in extraembryonic membrane and 18 other cell types or tissues.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0045216; P:cell-cell junction organization; IBA:GO_Central.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IBA:GO_Central.
DR   GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IBA:GO_Central.
DR   GO; GO:0150105; P:protein localization to cell-cell junction; IBA:GO_Central.
DR   CDD; cd00992; PDZ_signaling; 3.
DR   CDD; cd12027; SH3_ZO-2; 1.
DR   Gene3D; 2.30.42.10; -; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005417; ZO.
DR   InterPro; IPR005419; ZO-2.
DR   InterPro; IPR035598; ZO-2_SH3.
DR   PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR   PANTHER; PTHR13865:SF26; TIGHT JUNCTION PROTEIN ZO-2; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01599; ZONOCCLUDNS2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 3.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          63..150
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          317..395
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          516..597
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          611..676
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          781..883
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          180..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..948
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..988
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1198 AA;  135763 MW;  70F86B63C5AD385C CRC64;
     MTKFDLFFRE RNTTLLSSPC EWDWQPNCIS RNKYSTRHHR LEPTDSLPSQ APGMEELIWE
     QYTVTLQKDS KRGFGIAVSG GRDNPHFENG ETSIVISDVL SGGPADGLLQ ENDRVIMVNG
     TPMEDVPHSF AVQQLRKSGK IAAIVVKRPR KVQLAPLRGD SSSMDPDERV FHVMDDREEF
     DGRSARSGYS ERSWHSGNGG RSRSWENSPE RRLPHDQPRG RERSYSRERS RGRSLERGLD
     QDYRRDRSQG RSIDRDDGYD RGHRRDYSPS VEYSQRHSAN ARYEMKRSQS RDQLHSRSPT
     PEMRRRSEQR DIERPIDVLL TKSKSNEEYG LRLGSQIFIK EMTRTGLATK DGNLHEGDII
     LKINGTVTEN MSLADARKLI EKSRGKLQLV VLRDSKQTLI NIPSLHDSDS EIEDISEIES
     NRSFSPDERR TDFDYHSSNE KLKERTNSRE ETSNRLSKMG ATPTPFKSTG DIVTAVFQEN
     NKEPKYQEDP PVSQPKAAPR TFLRPSPEDE AIYGPNTKMV KFKKGDSVGL RLAGGNDVGI
     FVAGIQEGTS AEQEGLQEGD QILKVNTQDF RGLVREDAVL YLLEIPKGEM VTILAQSRAD
     VYRDILACGR GDSFFIRSHF ECEKESPQSL AFTRGEIFRV VDTLYDGKLG NWLAVRIGNE
     LEKGLIPNKS RAEQMASVQN AQRDNSGDRA DFWRMRGQRS GVKKNLRKSR EDLTAIVSVS
     TKFPAYERVL LREAGFKRPV VLFGPIADIA MEKLANELPD LFQTAKTEPK DAGSEKSSGV
     VRLNTVRQII EQNKHALLDV TPKAVDLLNY TQWFPVVIFF NPDSRQGVKT MRQRLNPTSN
     KSSRKLFDQA NKLKKTCAHL FTGTINLNST NDSWFGSLKD LIHQQQGEAV WVSEGKLEGM
     DDDMDDRMSY LTAMGADYLS CDSRLISDFE DTDGEGGAYT DNELDEPAEE PQVSSITRSS
     EPVLHEESIR KPSPEPRGQM RRAGSRDQLR DTSPPPAFKP EPPKAKLQNK DEPYDITKSY
     EYRPNNSVTA SNEIPGAATK PYVPPVPLKP AFGRSILKPS TPTFPSQENE EHRGNGEEAN
     NAPKSVLGKV KIFEKMDHKA RIQRMQELQE AQNARLEIAQ KHPDIYAVPI KAPKPDLNST
     QVTSFRPPEP QKPPSRLYQD SKGSYGSDIE EEEYRQQLSE HSKRGYYGQP ARYRDTEL
//
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